ID F7XX49_MOREP Unreviewed; 599 AA.
AC F7XX49;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071,
GN ECO:0000313|EMBL:AEI74675.1};
GN OrderedLocusNames=MEPCIT_001 {ECO:0000313|EMBL:AEI74675.1};
OS Moranella endobia (strain PCIT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Moranella.
OX NCBI_TaxID=903503 {ECO:0000313|EMBL:AEI74675.1, ECO:0000313|Proteomes:UP000000504};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCIT;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT mealybugs.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI74675.1, ECO:0000313|Proteomes:UP000000504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCIT {ECO:0000313|EMBL:AEI74675.1,
RC ECO:0000313|Proteomes:UP000000504};
RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested symbiosis of
RT mealybugs.";
RL Curr. Biol. 21:1366-1372(2011).
CC -!- FUNCTION: Required for accurate and efficient protein synthesis under
CC certain stress conditions. May act as a fidelity factor of the
CC translation reaction, by catalyzing a one-codon backward translocation
CC of tRNAs on improperly translocated ribosomes. Back-translocation
CC proceeds from a post-translocation (POST) complex to a pre-
CC translocation (PRE) complex, thus giving elongation factor G a second
CC chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC dependent manner. {ECO:0000256|HAMAP-Rule:MF_00071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00071}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00071}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
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DR EMBL; CP002243; AEI74675.1; -; Genomic_DNA.
DR RefSeq; WP_013975426.1; NC_015735.1.
DR AlphaFoldDB; F7XX49; -.
DR STRING; 903503.MEPCIT_001; -.
DR KEGG; men:MEPCIT_001; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_6; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000000504; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR CDD; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00071};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Reference proteome {ECO:0000313|Proteomes:UP000000504}.
FT DOMAIN 2..184
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 599 AA; 66614 MW; D4564B83E74B82D0 CRC64;
MKNIRNFSII AHINHGKSTL ADRLIQTCGG VSEHQIAAQM LDSMELERER GITIKAQSVT
LYYKASDGNI YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYKAM
EMDLEVVTVL NKIDLPTVEP DRVAQEIEDI IGLDATNAVR CSAKTGVGVY ELLERLIKDI
PPPSGDPAAP LQALIIDSWF DNYLGVVSLV CIKHGTLCKG DKIKVMSTGQ LYNADRLGIF
VPKRIERNFL NCGEVGWLVC TMKDINGAPV GDTMTLARQP AKEALPGFKK VKPQVYAGMF
PVRSDSYEEF RDALGKLSLN DASLFYEPEH STVLGFGFRC GFLGLLHMEI IQERLEREYN
LELITTAPTV IYEVLTTDDH TIYVDSPSKL PPLNKIAELR EPVAACHILL PQVYLGKVIK
LCIEKRGVQT TIIYHGKQVA LTYEIPMSEI VLDFFDRLQS ASSGYASLDY NFKSFKHSDM
VRVDVLINGE RVDALALIAN REQAPQRGRD LVDKLQELIP RQQFEIAIQA AIGNNIIARS
TIKQLRKNVL AKCYGGDVSR KKKLLQKQKK GKKRMKQVGN VALPQEAFLA ILHMGKKSK
//
